HSPA8, alternately known as HSC70 or HSP73, is a constitutively expressed member of the HSP70 superfamily. Although its primary role in cells appears to be that of a general chaperone for unfolded proteins, HSPA8 has also been identified as the uncoating ATPase responsible for removing clathrin from coated vesicles and may also play a role in stabilizing untranslated mRNAs. In addition to these "housekeeping" functions, HSPA8 may also have an important role in inducible cellular stress responses. For example, oxidative or thermal stress promotes the nuclear/nucleolar accumulation of HSPA8, where it forms a complex with the topoisomerase I complex and likely protects it from heat inactivation. HSPA8 is reportedly phosphorylated in response to DNA damage, but it remains unclear what effect, if any, this has on HSPA8 function. Numerous high throughput studies support this observation. For more information, please see the HSPA8 page in PhosphoSitePlus® at www.phosphosite.org.